Purification and characterization of some enzymatic properties of neuraminidase from Corynebacterium ulcerans.
Neuraminidase of Corynebacterium-ulcerans was purified by affinity chromatography using immobilized colominic acid preparations. Neuraminidase appears to be a thermolabile protein, molecular mass 70 000 Da. The pH optimum of 5.5 is independent of the substrate used; the optimal temperature is 37 degrees C, the Michaelis constant towards N-acetylneuraminosyllactose is 5.2 X 10(-4) M. Ca2+ and Ba2+ activated the enzyme, but Zn2+, Fe2+, and chelating agent EDTA were inhibitory. In our experiments the enzyme did not hydrolyse the (alpha - 2.6) or (alpha - 2.8) bonds of submaxillary pig mucin and colominic acid, respectively, but it hydrolysed such substrates as fetuin, ovomucin, orosomucoid and horse serum glycoproteins.
D002413:Cations, Divalent; D002846:Chromatography, Affinity; D003352:Corynebacterium / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D009439:Neuraminidase / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D002413:Cations, Divalent; D004492:Edetic Acid; D009439:Neuraminidase